Please use this identifier to cite or link to this item: http://hdl.handle.net/2080/2306
Full metadata record
DC FieldValueLanguage
dc.contributor.authorSaleem, M-
dc.contributor.authorMorlot, S-
dc.contributor.authorHohendahl, A-
dc.contributor.authorManzi, J-
dc.contributor.authorLenz, M-
dc.contributor.authorRoux, A-
dc.date.accessioned2015-04-28T06:42:37Z-
dc.date.available2015-04-28T06:42:37Z-
dc.date.issued2015-02-19-
dc.identifier.citationNature Communication; ISSN:2041-1723en_US
dc.identifier.issn2041-1723-
dc.identifier.uri10.1038/ncomms7249-
dc.identifier.urihttp://hdl.handle.net/2080/2306-
dc.descriptionCopyright belongs to publisheren_US
dc.description.abstractIn endocytosis, scaffolding is one of the mechanisms to create membrane curvature by moulding the membrane into the spherical shape of the clathrin cage. However, the impact of membrane elastic parameters on the assembly and shape of clathrin lattices has never been experimentally evaluated. Here, we show that membrane tension opposes clathrin polymerization. We reconstitute clathrin budding in vitro with giant unilamellar vesicles (GUVs), purified adaptors and clathrin. By changing the osmotic conditions, we find that clathrin coats cause extensive budding of GUVs under low membrane tension while polymerizing into shallow pits under moderate tension. High tension fully inhibits polymerization. Theoretically, we predict the tension values for which transitions between different clathrin coat shapes occur. We measure the changes in membrane tension during clathrin polymerization, and use our theoretical framework to estimate the polymerization energy from these data. Our results show that membrane tension controls clathrin-mediated budding by varying the membrane budding energyen_US
dc.language.isoenen_US
dc.publisherMacmillan Publishers Limiteden_US
dc.subjectMembrane elasticityen_US
dc.subjectPolymerization energyen_US
dc.subjectClathrinen_US
dc.titleA balance between membrane elasticity and polymerization energy sets the shape of spherical clathrin coatsen_US
dc.typeArticleen_US
Appears in Collections:Journal Articles

Files in This Item:
File Description SizeFormat 
Saleem_ncomms.pdf3.5 MBAdobe PDFView/Open


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.